Diversity of amyloid beta peptide actions

Area of Science:

• Neuroscience
• Biochemistry
• Pharmacology

Background:

• Amyloidogenic proteins, like amyloid beta peptides (Aβs), are implicated in incurable diseases, notably Alzheimer's disease (AD).
• Current AD research primarily focuses on reducing Aβs to prevent aggregation and neurodegeneration.
• Emerging evidence suggests Aβs may possess physiological functions, with pathological effects potentially arising from other disease states.

Purpose of the Study:

• To review the dual role of Aβs in health and disease.
• To explore the enzymatic modifications of Aβs contributing to aggregation.
• To investigate the potential of plant-derived compounds in managing Aβs.

Main Methods:

• Literature review of studies on amyloidogenesis and Alzheimer's disease.
• Analysis of enzymatic pathways involving glutaminyl cyclase and dipeptidyl peptidase IV in Aβ modification.
• Evaluation of experimental data on plant preparations' effects on Aβs.

Main Results:

• Aβs exhibit physiological functions, and their pathological effects may be disease-context dependent.
• Enzymatic modifications (e.g., by glutaminyl cyclase) enhance Aβ aggregation.
• Plant preparations demonstrated efficacy in maintaining the physiological, non-aggregated state of Aβs.

Conclusions:

• Shifting focus from Aβs removal to treating underlying diseases is proposed for AD therapy.
• Glutaminyl cyclase and dipeptidyl peptidase IV are potential therapeutic targets for AD.
• Flavonoids and plant-based preparations show promise as neuroprotective, anticancer, and antidiabetic agents.